Cloned (Comment) | Organism |
---|---|
gene LIA1, expression in Escherichia coli strain BL21(DE3) as GST-tagged protein | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
E113A | site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme | Saccharomyces cerevisiae |
E116A | site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme | Saccharomyces cerevisiae |
E116D | site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme | Saccharomyces cerevisiae |
E238A | site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme | Saccharomyces cerevisiae |
E271A | site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme | Saccharomyces cerevisiae |
E80A | site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme | Saccharomyces cerevisiae |
H112A | site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme | Saccharomyces cerevisiae |
H237A | site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme | Saccharomyces cerevisiae |
H270A | site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme | Saccharomyces cerevisiae |
H79A | site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | required, essential structural role for iron binding in addition to its contribution to the catalysis of hypusine formation in the eIF-5A precursor. Lia1 is an iron metalloenzyme. Determination of metal contents in purified enzyme samples, overview. The apoenzyme has a larger hydrodynamic size than the holoenzyme | Saccharomyces cerevisiae | |
additional information | Lia1 contains no cadmium, cobalt, chromium, copper, magnesium, manganese, nickel and zinc | Saccharomyces cerevisiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
additional information | - |
The apoenzyme has a larger hydrodynamic size than the holoenzyme | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | Saccharomyces cerevisiae | activation of eIF5A | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
additional information | Saccharomyces cerevisiae | Lia1 contains HEAT-like repeats with a role for mediating protein-protein interactions | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
gene YJR070C or LIA1 | - |
Purification (Comment) | Organism |
---|---|
recombinant GST-tagged Lia1 from Escherichia coli strain BL21(DE3) by two steps of glutathione affinity chromatography and gel filtration. Separation of iron-free and iron-bound forms by gel filtration and native electrophoresis | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | - |
Saccharomyces cerevisiae | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | activation of eIF5A | Saccharomyces cerevisiae | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
additional information | Lia1 contains HEAT-like repeats with a role for mediating protein-protein interactions | Saccharomyces cerevisiae | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | ability of Lia1 to undergo conformational changes, the active enzyme occurs in a stabilized and compact three-dimensional fold with bound metal. Loss of tertiary contacts upon iron displacement led to an elongated conformation of Lia1, in which the N- and C-terminal domains are no longer in close proximity to guarantee the proper orientation of the active groups within the active site pocket. Lia1 contains HEAT-like repeats with a role for mediating protein-protein interactions. Structure spectral analysis of iron-free and iron-bound enzyme, and effects of pH on Lia1 catalytic activity and tertiary structure, overview | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
deoxyhypusine hydroxylase | - |
Saccharomyces cerevisiae |
Lia1 | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
metabolism | the unique amino acid hypusine is formed exclusively in eIF5A by the successive action of deoxyhypusine synthase and deoxyhypusine hydroxylase | Saccharomyces cerevisiae |
physiological function | the enzyme activates eIF5A, that plays a role in the elongation step of translation | Saccharomyces cerevisiae |